4DFG
Crystal Structure of Wild-type HIV-1 Protease with Cyclopentyltetrahydro- furanyl Urethanes as P2-ligand, GRL-0249A
Summary for 4DFG
| Entry DOI | 10.2210/pdb4dfg/pdb |
| Related | 2HB3 2IEN 2Z4O 3DJK 3DK1 3H5B 3I6O 3OK9 3ST5 |
| Descriptor | Protease, SODIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | aspartic acid protease, hiv-1 protease inhibitor grl-0249a, cyclopentyltetrahydro- furanyl urethanes p2-ligands, wild-type hiv-1 protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03367 |
| Total number of polymer chains | 2 |
| Total formula weight | 22302.90 |
| Authors | Wang, Y.-F.,Agniswamy, J.,Weber, I.T. (deposition date: 2012-01-23, release date: 2012-03-21, Last modification date: 2023-09-13) |
| Primary citation | Ghosh, A.K.,Chapsal, B.D.,Steffey, M.,Agniswamy, J.,Wang, Y.F.,Amano, M.,Weber, I.T.,Mitsuya, H. Substituent effects on P2-cyclopentyltetrahydrofuranyl urethanes: Design, synthesis, and X-ray studies of potent HIV-1 protease inhibitors. Bioorg.Med.Chem.Lett., 22:2308-2311, 2012 Cited by PubMed Abstract: The design, synthesis, and biological evaluation of novel C3-substituted cyclopentyltetrahydrofuranyl (Cp-THF)-derived HIV-1 protease inhibitors are described. Various C3-functional groups on the Cp-THF ligand were investigated in order to maximize the ligand-binding site interactions in the flap region of the protease. Inhibitors 3c and 3d have displayed the most potent enzyme inhibitory and antiviral activity. Both inhibitors have maintained impressive activity against a panel of multidrug resistant HIV-1 variants. A high-resolution X-ray crystal structure of 3c-bound HIV-1 protease revealed a number of important molecular insights into the ligand-binding site interactions. PubMed: 22364812DOI: 10.1016/j.bmcl.2012.01.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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